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Atomistry » Chlorine » PDB 4ui0-4uuq » 4usv » |
Chlorine in PDB 4usv: Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Atp and CalciumEnzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Atp and Calcium
All present enzymatic activity of Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Atp and Calcium:
4.6.1.1; Protein crystallography data
The structure of Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Atp and Calcium, PDB code: 4usv
was solved by
S.Kleinboelting,
C.Steegborn,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4usv:
The structure of Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Atp and Calcium also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Atp and Calcium
(pdb code 4usv). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Atp and Calcium, PDB code: 4usv: Chlorine binding site 1 out of 1 in 4usvGo back to Chlorine Binding Sites List in 4usv
Chlorine binding site 1 out
of 1 in the Crystal Structure of Human Soluble Adenylyl Cyclase with Pyrophosphate Resulting From Soaking with Atp and Calcium
Mono view Stereo pair view
Reference:
S.Kleinbolting,
J.Van Den Heuvel,
C.Steegborn.
Structural Analysis of Human Soluble Adenylyl Cyclase and Crystal Structures of Its Nucleotide Complexes - Implications For Cyclase Catalysis and Evolution. Febs J. V. 281 4151 2014.
Page generated: Sat Dec 12 11:16:14 2020
ISSN: ISSN 1742-464X PubMed: 25040695 DOI: 10.1111/FEBS.12913 |
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